메뉴 건너뛰기




Volumn 11, Issue 2, 2004, Pages 121-127

The enzymes and control of eukaryotic mRNA turnover

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLOBIN; ENDONUCLEASE; EXONUCLEASE; MESSENGER RNA; MESSENGER RNA DEADENYLASE; NUCLEASE; POLYADENYLIC ACID; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 0742288008     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb724     Document Type: Review
Times cited : (678)

References (105)
  • 1
    • 0032727868 scopus 로고    scopus 로고
    • The exosome: A proteasome for RNA?
    • van Hoof, A. & Parker, R. The exosome: a proteasome for RNA? Cell 99, 347-350 (1999).
    • (1999) Cell , vol.99 , pp. 347-350
    • Van Hoof, A.1    Parker, R.2
  • 2
    • 0037686295 scopus 로고    scopus 로고
    • Killing the messenger: Short RNAs that silence gene expression
    • Dykxhoorn, D.M., Novina, C.D. & Sharp, P.A. Killing the messenger: short RNAs that silence gene expression. Nat. Rev. Mol. Cell Biol. 4, 457-467 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 457-467
    • Dykxhoorn, D.M.1    Novina, C.D.2    Sharp, P.A.3
  • 3
    • 0035951432 scopus 로고    scopus 로고
    • Quality control of mRNA function
    • Maquat, L.E. & Carmichael, G.G. Quality control of mRNA function. Cell 26, 173-176 (2000).
    • (2000) Cell , vol.26 , pp. 173-176
    • Maquat, L.E.1    Carmichael, G.G.2
  • 4
    • 0033790503 scopus 로고    scopus 로고
    • Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae
    • Tucker, M. & Parker, R. Mechanisms and control of mRNA decapping in Saccharomyces cerevisiae. Annu. Rev. Biochem. 69, 571-595 (2000).
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 571-595
    • Tucker, M.1    Parker, R.2
  • 6
    • 0000577868 scopus 로고    scopus 로고
    • The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SK12 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex
    • Anderson, J.S.J. & Parker, R. The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SK12 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J. 17, 1497-1506 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1497-1506
    • Anderson, J.S.J.1    Parker, R.2
  • 7
    • 18044371822 scopus 로고    scopus 로고
    • AU bindng proteins recruit the exosome to degrade ARE-containing mRNAs
    • Chen, C.Y. et al. AU bindng proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 107, 451-464 (2001).
    • (2001) Cell , vol.107 , pp. 451-464
    • Chen, C.Y.1
  • 8
    • 0035861864 scopus 로고    scopus 로고
    • Furctional link between the mammalian exosome and mRNA decapping
    • Wang, Z. & Kiledjian, M. Furctional link between the mammalian exosome and mRNA decapping. Cell 107, 751-762 (2001).
    • (2001) Cell , vol.107 , pp. 751-762
    • Wang, Z.1    Kiledjian, M.2
  • 9
    • 0037080834 scopus 로고    scopus 로고
    • The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements
    • Mukherjee, D. et al. The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21, 165-174 (2002).
    • (2002) EMBO J. , vol.21 , pp. 165-174
    • Mukherjee, D.1
  • 10
    • 0037009517 scopus 로고    scopus 로고
    • The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases
    • Liu, H., Rodgers, N.D., Jiao, X. & Kiledjian, M. The scavenger mRNA decapping enzyme DcpS is a member of the HIT family of pyrophosphatases. EMBO J. 21, 4699-4708 (2002).
    • (2002) EMBO J. , vol.21 , pp. 4699-4708
    • Liu, H.1    Rodgers, N.D.2    Jiao, X.3    Kiledjian, M.4
  • 11
    • 0036053733 scopus 로고    scopus 로고
    • Regulation of pathways of mRNA destabilization and stabilizatior
    • Dodson, R.E. & Shapiro, D.J. Regulation of pathways of mRNA destabilization and stabilizatior. Prog. Nucleic Acid Res. Mol. Biol. 72, 129-164 (2002).
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.72 , pp. 129-164
    • Dodson, R.E.1    Shapiro, D.J.2
  • 12
    • 0037154977 scopus 로고    scopus 로고
    • Nuclear RNA turnover
    • Moore, M.J. Nuclear RNA turnover. Cell 108, 431-434 (2002).
    • (2002) Cell , vol.108 , pp. 431-434
    • Moore, M.J.1
  • 13
    • 0027932513 scopus 로고
    • Premature translational termination triggers mRNA decapping
    • Muhlrad, D. & Parker, R. Premature translational termination triggers mRNA decapping. Nature 370, 578-581 (1994).
    • (1994) Nature , vol.370 , pp. 578-581
    • Muhlrad, D.1    Parker, R.2
  • 14
    • 0038402506 scopus 로고    scopus 로고
    • Computational modeling and experimental analysis of nonsense-mediated decay in yeast
    • Cao, D. & Parker, R. Computational modeling and experimental analysis of nonsense-mediated decay in yeast. Cell 113, 533-545 (2003).
    • (2003) Cell , vol.113 , pp. 533-545
    • Cao, D.1    Parker, R.2
  • 15
    • 0037762554 scopus 로고    scopus 로고
    • An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′→5′ degradation
    • Mitchell, P. & Tollervey, D. An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′→5′ degradation. Mol. Cell 11, 1405-1413 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1405-1413
    • Mitchell, P.1    Tollervey, D.2
  • 16
    • 0041524062 scopus 로고    scopus 로고
    • Interaction between Ski7p and Upf1p is required for nonsense-mediated 3′-to-5′ mRNA decay in yeast
    • Takahashi, S., Araki, Y., Sakuno, T. & Katada, T. Interaction between Ski7p and Upf1p is required for nonsense-mediated 3′-to-5′ mRNA decay in yeast. EMBO J. 22, 3951-3959 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3951-3959
    • Takahashi, S.1    Araki, Y.2    Sakuno, T.3    Katada, T.4
  • 17
    • 0037155592 scopus 로고    scopus 로고
    • An mRNA surveillance mechanism that eliminates transcripts lacking termination codons
    • Frischmeyer, P.A. et al. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295, 2258-2261 (2002).
    • (2002) Science , vol.295 , pp. 2258-2261
    • Frischmeyer, P.A.1
  • 18
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof, A., Frischmeyer, P.A., Dietz, H.C. & Parker, R. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295, 2262-2264 (2002).
    • (2002) Science , vol.295 , pp. 2262-2264
    • Van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 19
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated proteins Ccr 4 and Caf1 are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
    • Tucker, M. et al. The transcription factor associated proteins Ccr4 and Caf1 are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104, 377-386 (2001).
    • (2001) Cell , vol.104 , pp. 377-386
    • Tucker, M.1
  • 20
    • 0347323165 scopus 로고    scopus 로고
    • The CCR4-NOT complex plays diverse roles in mRNA metabolism
    • Denis, C.L & Chen, J. The CCR4-NOT complex plays diverse roles in mRNA metabolism. Prog. Nucleic Acid Res. Mol. Biol. 73, 221-250 (2003).
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 221-250
    • Denis, C.L.1    Chen, J.2
  • 21
    • 0034213216 scopus 로고    scopus 로고
    • 2+-dependent endonucleases
    • 2+-dependent endonucleases. Trends Biochem. Sci. 25, 272-273 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 272-273
    • Drakic, M.1
  • 22
    • 0037086657 scopus 로고    scopus 로고
    • Ccr4p is the catalytic sub-unit of a Ccr4/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae
    • Tucker, M., Staples, R.R., Valencia-Sanchez, M.A., Muhlrad, D. & Parker, R Ccr4p is the catalytic sub-unit of a Ccr4/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. EMBO J. 21, 1427-1436 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1427-1436
    • Tucker, M.1    Staples, R.R.2    Valencia-Sanchez, M.A.3    Muhlrad, D.4    Parker, R.5
  • 23
    • 0037086701 scopus 로고    scopus 로고
    • CCR4, a 3′-5′ poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase
    • Chen, J., Chiang, Y.C. & Denis, C.L. CCR4, a 3′-5′ poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase. EMBO J. 21, 1414-1426 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1414-1426
    • Chen, J.1    Chiang, Y.C.2    Denis, C.L.3
  • 24
    • 0037316406 scopus 로고    scopus 로고
    • Nocturnin, a deadenylase in Xenopus laevis retina. A mechanism for posttranscriptional control of circadian-related mRNA
    • Baggs, J.E. & Green, C.B. Nocturnin, a deadenylase in Xenopus laevis retina. A mechanism for posttranscriptional control of circadian-related mRNA. Curr. Biol. 13, 189-198 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 189-198
    • Baggs, J.E.1    Green, C.B.2
  • 25
    • 0035875115 scopus 로고    scopus 로고
    • The yeast POP 2 gene encodes a nuclease involved in mRNA deadenylation
    • Daugeron, M.C., Mauxion, F. & Seraphin, B. The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation. Nucleic Acids Res. 29, 2448-2455 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2448-2455
    • Daugeron, M.C.1    Mauxion, F.2    Seraphin, B.3
  • 26
    • 0345832225 scopus 로고    scopus 로고
    • X-ray structure and activity of the yeast Pop2 protein: A nuclease subunit of the mRNA deadenylase complex
    • Thore, S., Mauxion, F., Séraphin, B & Suck, D. X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex. EMBO Rep. 4, 1150-1155 (2003).
    • (2003) EMBO Rep. , vol.4 , pp. 1150-1155
    • Thore, S.1    Mauxion, F.2    Séraphin, B.3    Suck, D.4
  • 27
    • 0031574363 scopus 로고    scopus 로고
    • The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains
    • Moser, M.J., Holley, W.R., Chatterjee, A. & Mian, I.S. The proofreading domain of Escherichia coli DNA polymerase I and other DNA and/or RNA exonuclease domains. Nucleic Acids Res. 25, 5110-5118 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5110-5118
    • Moser, M.J.1    Holley, W.R.2    Chatterjee, A.3    Mian, I.S.4
  • 28
    • 0028881713 scopus 로고
    • Polymerase structures and function: Variations on a theme?
    • , Joyce, C.M. & Steitz, T.A. Polymerase structures and function: variations on a theme? J. Bacteriol. 177, 6321-6329 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 29
    • 0031740339 scopus 로고    scopus 로고
    • Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation
    • Brown, C.E. & Sachs, A.B. Poly(A) tail length control in Saccharomyces cerevisiae occurs by message-specific deadenylation. Mol. Cell. Biol. 18, 6548-6559 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6548-6559
    • Brown, C.E.1    Sachs, A.B.2
  • 30
    • 0037151028 scopus 로고    scopus 로고
    • Posttranscriptional regulation of the RAD5 DNA repair gene by the dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks
    • Hammet, A., Pike, B.L. & Heierhorst, J. Posttranscriptional regulation of the RAD5 DNA repair gene by the dun1 kinase and the Pan2-Pan3 poly(A)-nuclease complex contributes to survival of replication blocks. J. Biol. Chem. 277, 22469-22474 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 22469-22474
    • Hammet, A.1    Pike, B.L.2    Heierhorst, J.3
  • 31
    • 0035836765 scopus 로고    scopus 로고
    • A comprehensive two-hybrid analysis to explore the yeast protein interactome
    • Ito, T. et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Pro. Natl. Acad. Sci. USA 98, 4277-4278 (2001).
    • (2001) Pro. Natl. Acad. Sci. USA , vol.98 , pp. 4277-4278
    • Ito, T.1
  • 32
    • 0026630153 scopus 로고
    • Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA
    • Åström, J., Åström, A. & Virtanen, A. Properties of a HeLa cell 3′ exonuclease specific for degrading poly(A) tails of mammalian mRNA. J. Biol. Chem. 267, 18154-18159 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 18154-18159
    • Åström, J.1    Åström, A.2    Virtanen, A.3
  • 33
    • 0039535081 scopus 로고    scopus 로고
    • Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease
    • Körner, C.G. & Wahle. E. Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease. J. Biol. Chem. 272, 10448-10456 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 10448-10456
    • Körner, C.G.1    Wahle, E.2
  • 35
    • 0038751970 scopus 로고    scopus 로고
    • Tristetraprolin and its family members can promote the cell-free deadenylatior of AU-rich element-containing mRNAs by poly(A) ribonuclease
    • Lai, W.S., Kennington, E.A. & Blackshear, P.J. Tristetraprolin and its family members can promote the cell-free deadenylatior of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol. Cell. Biol. 23, 3798-3812 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3798-3812
    • Lai, W.S.1    Kennington, E.A.2    Blackshear, P.J.3
  • 36
    • 0033680082 scopus 로고    scopus 로고
    • Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro
    • Gao, M., Fritz, D.T., Ford, L.P. & Wilusz, J. Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro. Mol. Cell 5, 479-488 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 479-488
    • Gao, M.1    Fritz, D.T.2    Ford, L.P.3    Wilusz, J.4
  • 37
    • 0040126630 scopus 로고    scopus 로고
    • The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes
    • Körner, C.G. et al. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 17, 5427-5437 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5427-5437
    • Körner, C.G.1
  • 38
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune, F., Li, X. & Maquat, L.E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12, 675-687 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 39
    • 0037675801 scopus 로고    scopus 로고
    • Identification of multiple RNA features that influence CCR 4 deadenylation activity
    • Viswanathan, P., Chen, J., Chiang, Y.-C. & Denis, C.L. Identification of multiple RNA features that influence CCR4 deadenylation activity. J. Biol. Chem. 278, 14949-14955 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14949-14955
    • Viswanathan, P.1    Chen, J.2    Chiang, Y.-C.3    Denis, C.L.4
  • 41
    • 0035958843 scopus 로고    scopus 로고
    • The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation
    • Martînez, J., Ren, Y.-G., Nilsson, P., Ehrenberg, M. & Virtanen, A. The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J. Biol. Chem. 276, 27923-27929 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27923-27929
    • Martînez, J.1    Ren, Y.-G.2    Nilsson, P.3    Ehrenberg, M.4    Virtanen, A.5
  • 42
    • 0026800718 scopus 로고
    • Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast
    • Sach, A.B. & Deardorff, J.A. Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast. Cell 70, 961-973 (1992).
    • (1992) Cell , vol.70 , pp. 961-973
    • Sach, A.B.1    Deardorff, J.A.2
  • 43
    • 0036498828 scopus 로고    scopus 로고
    • A PUF family portrait: 3′UTR regulation as a way of life
    • Wickens, M., Bernstein, D.S., Kimble, J. & Parker, R. A PUF family portrait: 3′UTR regulation as a way of life. Trends Genet. 18, 150-157 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 150-157
    • Wickens, M.1    Bernstein, D.S.2    Kimble, J.3    Parker, R.4
  • 44
    • 0033785798 scopus 로고    scopus 로고
    • Musing on the structural organization of the exosome complex
    • Mitchell, P. & Tollervey, D. Musing on the structural organization of the exosome complex. Nat. Struct. Biol. 7, 843-846 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 843-846
    • Mitchell, P.1    Tollervey, D.2
  • 45
    • 0036469214 scopus 로고    scopus 로고
    • The yin and yang of the exosome
    • , Butler, J.S. The yin and yang of the exosome. Trends Cell Biol. 12, 90-96 (2002).
    • (2002) Trends Cell Biol. , vol.12 , pp. 90-96
    • Butler, J.S.1
  • 47
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons, M.F., Jones, G.H. & Luisi, B.F. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure Fold Des. 8, 1215-1226 (2000).
    • (2000) Structure Fold Des. , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 48
    • 0036023943 scopus 로고    scopus 로고
    • A complex prediction: Three-dimensional model of the yeast exosome
    • Aloy, P. et al. A complex prediction: three-dimensional model of the yeast exosome. EMBO Rep. 3, 628-635 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 628-635
    • Aloy, P.1
  • 49
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′→5′cleases exoribonucleases
    • Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. & Tollervey, D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′→5′cleases exoribonucleases. Cell 91, 457-466 (1997).
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 50
    • 0034118002 scopus 로고    scopus 로고
    • The yeast antiviral proteins Ski2p, Ski3p, and Ski 8p exist as a complex in vivo
    • Brown, J.T., Bai, X. & Johnson, A.W. The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in vivo. RNA 6, 449-457 (2000).
    • (2000) RNA , vol.6 , pp. 449-457
    • Brown, J.T.1    Bai, X.2    Johnson, A.W.3
  • 51
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: From generic motors to specific dissociation functions
    • Tanner, N.K. & Linder, P. DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell 8, 251-262 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 52
    • 0033555659 scopus 로고    scopus 로고
    • ELAV proteins stabilize deadenylated intermediates in a rovel in vitro mRNA deadenylation/degradation system
    • Ford, L.P., Watson, J., Keene, J.D. & Wilusz, J. ELAV proteins stabilize deadenylated intermediates in a rovel in vitro mRNA deadenylation/degradation system. Genes Dev. 13, 188-201 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 188-201
    • Ford, L.P.1    Watson, J.2    Keene, J.D.3    Wilusz, J.4
  • 53
    • 0035801392 scopus 로고    scopus 로고
    • Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast
    • Araki, Y. et al. Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast. EMBO J. 20, 4684-4693 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4684-4693
    • Araki, Y.1
  • 55
    • 0017368368 scopus 로고
    • 7G(5′)PN-pyrophosphatase activity from HeLa cells
    • 7G(5′)PN-pyrophosphatase activity from HeLa cells. J. Biol. Chem. 252, 2815-2821 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 2815-2821
    • Nuss, D.L.1    Furuichi, Y.2
  • 56
    • 0026573613 scopus 로고
    • Purification and properties of a decapping enzyme from rat liver cytosol
    • Kumagai, H. et al. Purification and properties of a decapping enzyme from rat liver cytosol. Biochim. Biophys. Acta 1119, 45-51 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 45-51
    • Kumagai, H.1
  • 57
    • 0033847384 scopus 로고    scopus 로고
    • The pory(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity
    • Wang, Z. & Kiredjian, M. The pory(A)-binding protein and an mRNA stability protein jointly regulate an endoribonuclease activity. Mol. Cell. Biol. 20, 6334-6341 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6334-6341
    • Wang, Z.1    Kiredjian, M.2
  • 58
    • 0142027794 scopus 로고    scopus 로고
    • DcpS can act in the 5′-3′ mRNA decay pathway in addition to the 3′-5′ pathway
    • van Dijk, E., Hir, H.L. & Séraphin, B. DcpS can act in the 5′-3′ mRNA decay pathway in addition to the 3′-5′ pathway. Proc. Natl. Acad. Sci. USA 100, 12081-12086 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12081-12086
    • Van Dijk, E.1    Hir, H.L.2    Séraphin, B.3
  • 59
    • 0033214061 scopus 로고    scopus 로고
    • The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
    • Dunckley, T. & Parker, R. The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J. 18, 5411-5422 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5411-5422
    • Dunckley, T.1    Parker, R.2
  • 60
    • 0029758321 scopus 로고    scopus 로고
    • An essential component of the decapping enzyme required for normal rates of mRNA decay in yeast
    • Beelman, C.A. et al. An essential component of the decapping enzyme required for normal rates of mRNA decay in yeast. Nature 382, 642-646 (1996).
    • (1996) Nature , vol.382 , pp. 642-646
    • Beelman, C.A.1
  • 62
    • 0035148534 scopus 로고    scopus 로고
    • Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae
    • Dunckley, T., Tucker, M. & Parker, R. Two related proteins, Edc1p and Edc2p, stimulate mRNA decapping in Saccharomyces cerevisiae. Genetics 257, 27-37 (2001).
    • (2001) Genetics , vol.257 , pp. 27-37
    • Dunckley, T.1    Tucker, M.2    Parker, R.3
  • 63
    • 0036888905 scopus 로고    scopus 로고
    • Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
    • Lykke-Andersen, J. Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol. Cell. Biol. 22, 8114-8121 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8114-8121
    • Lykke-Andersen, J.1
  • 64
    • 0019180695 scopus 로고
    • An mRNA decapping enzyme from ribosomes of Saccharomyces cerevisiae
    • Stevens, A. An mRNA decapping enzyme from ribosomes of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 96, 1150-1055 (1980).
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 1150-1055
    • Stevens, A.1
  • 66
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk, E. et al. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21, 6915-6924 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1
  • 67
    • 0023164983 scopus 로고
    • A 5′-3′ exoribonuclease of Saccharomyces cerevisiae: Size and novel substrate specificity
    • Stevens, A. & Maupin, M.K. A 5′-3′ exoribonuclease of Saccharomyces cerevisiae: size and novel substrate specificity. Arch. Biochem. Biophys. 252, 339-347 (1987).
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 339-347
    • Stevens, A.1    Maupin, M.K.2
  • 68
    • 0027522193 scopus 로고
    • A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses
    • Koonin, E.V. A highly conserved sequence motif defining the family of MutT-related proteins from eubacteria, eukaryotes and viruses. Nucleic Acids Res. 21, 4847 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4847
    • Koonin, E.V.1
  • 69
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or 'Nudix' hydrolases, a family of versatile, widely distributed, 'housecleaning' enzymes
    • Bessman, M.J., Frick, D.N. & O'Handley, S.F. The MutT proteins or 'Nudix' hydrolases, a family of versatile, widely distributed, 'housecleaning' enzymes. J. Biol. Chem. 271, 25059-25062 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 70
    • 0037157144 scopus 로고    scopus 로고
    • An EVH1/WH1 domain as a key actor in TGFB signalling
    • Callebaut, I. An EVH1/WH1 domain as a key actor in TGFB signalling. FEBS Lett. 519, 178-180 (2002).
    • (2002) FEBS Lett. , vol.519 , pp. 178-180
    • Callebaut, I.1
  • 71
    • 1442360375 scopus 로고    scopus 로고
    • Crystal structure of Dcp1p and its functional implications in mRNA Decapping
    • in the press
    • She, M. et al. Crystal structure of Dcp1p and its functional implications in mRNA Decapping Nat. Struct. Mol. Biol. (in the press).
    • Nat. Struct. Mol. Biol.
    • She, M.1
  • 72
    • 0037138362 scopus 로고    scopus 로고
    • EVH1 domains: Structure, function and interactions
    • Ball, L.J., Jarchau, T., Oschkinat, H. & Walter, U. EVH1 domains: structure, function and interactions. FEBS Lett. 513, 45-52 (2002).
    • (2002) FEBS Lett. , vol.513 , pp. 45-52
    • Ball, L.J.1    Jarchau, T.2    Oschkinat, H.3    Walter, U.4
  • 73
    • 0041832085 scopus 로고    scopus 로고
    • Functional characterization of the mammalian mRNA decapping enzyme hDcp2
    • Piccirillo, C., Khanna, R. & Kiledjian, M. Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA 9, 1138-1147 (2003).
    • (2003) RNA , vol.9 , pp. 1138-1147
    • Piccirillo, C.1    Khanna, R.2    Kiledjian, M.3
  • 74
    • 0032473359 scopus 로고    scopus 로고
    • Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme
    • LaGrandeur, T.E. & Parker, R. Isolation and characterization of Dcp1p, the yeast mRNA decapping enzyme. EMBO J. 17, 1487-1496 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1487-1496
    • LaGrandeur, T.E.1    Parker, R.2
  • 75
    • 0028809873 scopus 로고
    • Multiple functions of the poly(A) binding protein in mRNA decapping and deadenylation
    • Caponigro, G. & Parker, R. Multiple functions of the poly(A) binding protein in mRNA decapping and deadenylation. Genes Dev. 9, 2421-2432 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 2421-2432
    • Caponigro, G.1    Parker, R.2
  • 76
    • 0032532439 scopus 로고    scopus 로고
    • mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation
    • Coller, J.M., Gray, N.K. & Wickens, M.P. mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation. Genes Dev 12, 3226-3235 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 3226-3235
    • Coller, J.M.1    Gray, N.K.2    Wickens, M.P.3
  • 77
    • 0034761729 scopus 로고    scopus 로고
    • Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts
    • Wilusz, C.J. et al. Poly(A)-binding proteins regulate both mRNA deadenylation and decapping in yeast cytoplasmic extracts. RNA 7, 1416-1424 (2001).
    • (2001) RNA , vol.7 , pp. 1416-1424
    • Wilusz, C.J.1
  • 78
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor elF-4G
    • Tarun, S.Z. Jr. & Sachs, A.B. Association of the yeast poly(A) tail binding protein with translation initiation factor elF-4G. EMBO J. 16, 7168-7177 (1996).
    • (1996) EMBO J. , vol.16 , pp. 7168-7177
    • Tarun Jr., S.Z.1    Sachs, A.B.2
  • 79
    • 0032778953 scopus 로고    scopus 로고
    • Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of yeast mRNAs
    • Schwartz, D. & Parker, R. Mutations in translation initiation factors lead to increased rates of deadenylation and decapping of yeast mRNAs. Mol. Cell. Biol. 19, 5247-5256 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5247-5256
    • Schwartz, D.1    Parker, R.2
  • 80
    • 0033773044 scopus 로고    scopus 로고
    • mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E
    • Schwartz, D. & Parker, R. mRNA decapping in yeast requires dissociation of the cap binding protein, eukaryotic translation initiation factor 4E. Mol. Cell. Biol. 20, 7933-7942 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7933-7942
    • Schwartz, D.1    Parker, R.2
  • 81
    • 0742270826 scopus 로고    scopus 로고
    • Poly(A)-binding protein mediated regulation of hDcp2 decapping
    • in press
    • Khanna, R. & Kiledjian, M. Poly(A)-binding protein mediated regulation of hDcp2 decapping. Genes Dev. (2004, in press).
    • (2004) Genes Dev
    • Khanna, R.1    Kiledjian, M.2
  • 82
    • 0033066673 scopus 로고    scopus 로고
    • An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro
    • Wang, Z., Day, N., Trifillis, P. & Kiledjian, M. An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Mol. Cell. Biol. 19, 4552-4560 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4552-4560
    • Wang, Z.1    Day, N.2    Trifillis, P.3    Kiledjian, M.4
  • 83
    • 0034663782 scopus 로고    scopus 로고
    • The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the elF4F translation initiation complex
    • Vilela, C., Velasco, C., Ptushkina, M. & McCarthy, J.E., The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the elF4F translation initiation complex. EMBO J. 19, 4372-4382 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4372-4382
    • Vilela, C.1    Velasco, C.2    Ptushkina, M.3    McCarthy, J.E.4
  • 84
    • 0035930337 scopus 로고    scopus 로고
    • Targeting an mRNA for decapping: Displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs
    • Tharun, S. & Parker, R. Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs. Mol. Cell 8, 1075-1083 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 1075-1083
    • Tharun, S.1    Parker, R.2
  • 85
    • 0037968357 scopus 로고    scopus 로고
    • Decapping and decay of messenger RNA occur in cytoplasmic processing bodies
    • Sheth, U. & R. Parker, R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 300, 805-808 (2003).
    • (2003) Science , vol.300 , pp. 805-808
    • Sheth, U.1    Parker, R.2
  • 86
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrn1 in distinct cytoplasmic foci
    • Ingelfinger, D., Arndt-Jovin, D.J., Luhrmann, R. & Achset, T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrn1 in distinct cytoplasmic foci. RNA 8, 1489-1501 (2002).
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achset, T.4
  • 87
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • Bashkirov, V.I., Scherthan, H., Solinger, J.A., Buerstedde, J.M. & Heyer, W.D. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 136, 761-773 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.M.4    Heyer, W.D.5
  • 88
    • 0028225993 scopus 로고
    • Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA
    • Beelman, C. A. & Parker, R. Differential effects of translational inhibition in cis and in trans on the decay of the unstable yeast MFA2 mRNA. J. Biol. Chem. 269, 9687-9692 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 9687-9692
    • Beelman, C.A.1    Parker, R.2
  • 89
    • 0031841817 scopus 로고    scopus 로고
    • Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant
    • Boeck, R., Lapeyre, P., Brown, C.E. & Sachs, A.B. Capped mRNA degradation intermediates accumulate in the yeast spb8-2 mutant. Mol. Cell. Biol. 18, 5062-5072 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5062-5072
    • Boeck, R.1    Lapeyre, P.2    Brown, C.E.3    Sachs, A.B.4
  • 90
    • 0034732089 scopus 로고    scopus 로고
    • Yeast Sm-like proteins function in mRNA decapping and decay
    • Tharun, S. et al. Yeast Sm-like proteins function in mRNA decapping and decay. Nature 404, 515-518 (2000).
    • (2000) Nature , vol.404 , pp. 515-518
    • Tharun, S.1
  • 91
    • 0034599976 scopus 로고    scopus 로고
    • A Sm-like protein complex that participates in mRNA degradation
    • Bouveret, E., Rigaut, G., Shevchenko, A., Wilm, M. & Seraphin, B. A Sm-like protein complex that participates in mRNA degradation. EMBO J. 19, 1661-1671 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1661-1671
    • Bouveret, E.1    Rigaut, G.2    Shevchenko, A.3    Wilm, M.4    Seraphin, B.5
  • 92
    • 0033866402 scopus 로고    scopus 로고
    • The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p
    • Bonnerot, C., Boeck, R. & Lapeyre, B. The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required for mRNA decay, and are functionally linked to Pab1p. Mol. Cell. Biol. 20, 5939-5946 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5939-5946
    • Bonnerot, C.1    Boeck, R.2    Lapeyre, B.3
  • 93
    • 0035674477 scopus 로고    scopus 로고
    • The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes
    • Coller, J.M., Tucker, M., Sheth, U., Valencia-Sanchez, M.A. & Parker, R. The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes. RNA 7, 1717-1727 (2001).
    • (2001) RNA , vol.7 , pp. 1717-1727
    • Coller, J.M.1    Tucker, M.2    Sheth, U.3    Valencia-Sanchez, M.A.4    Parker, R.5
  • 94
    • 0037013898 scopus 로고    scopus 로고
    • The DEAD box protein Dhh 1 stimulates the decapping enzyme Dcp1
    • Fischer, N. & Weis, K. The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1. EMBO J. 21, 2788-2797 (2002).
    • (2002) EMBO J. , vol.21 , pp. 2788-2797
    • Fischer, N.1    Weis, K.2
  • 95
    • 0028948708 scopus 로고
    • Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen
    • He, F. & Jacobson, A. Identification of a novel component of the nonsense-mediated mRNA decay pathway by use of an interacting protein screen. Genes Dev. 9, 437-454 (1995).
    • (1995) Genes Dev. , vol.9 , pp. 437-454
    • He, F.1    Jacobson, A.2
  • 96
    • 0742305519 scopus 로고    scopus 로고
    • Edc3p, a novel conserved protein, enhances mRNA decay in Yeast
    • in the press
    • Kshirsagar, M. & Parker, R. Edc3p, a novel conserved protein, enhances mRNA decay in Yeast. Genetics (in the press).
    • Genetics
    • Kshirsagar, M.1    Parker, R.2
  • 97
    • 0037322952 scopus 로고    scopus 로고
    • The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate activity of the decapping enzyme
    • Schwartz, D., Decker, C.J. & Parker, R The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate activity of the decapping enzyme. RNA 9, 239-251 (2003).
    • (2003) RNA , vol.9 , pp. 239-251
    • Schwartz, D.1    Decker, C.J.2    Parker, R.3
  • 98
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′ to 3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • Hsu, C. & Stevens, A. Yeast cells lacking 5′ to 3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol. 13, 4826-4835 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4826-4835
    • Hsu, C.1    Stevens, A.2
  • 99
    • 0032525327 scopus 로고    scopus 로고
    • A single amino acid substitution in yeast elF5A results in mRNA stabilization
    • Zuk, D. & Jacobson, A. A single amino acid substitution in yeast elF5A results in mRNA stabilization, EMBO J. 17, 2914-2925 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2914-2925
    • Zuk, D.1    Jacobson, A.2
  • 100
    • 0032415357 scopus 로고    scopus 로고
    • Identification and developmental expression of a 5′-3′ exoribonuclease from Drosophila melanogaster
    • Till, D.D., et al. Identification and developmental expression of a 5′-3′ exoribonuclease from Drosophila melanogaster. Mech. Dev. 79, 51-55 (1998).
    • (1998) Mech. Dev. , vol.79 , pp. 51-55
    • Till, D.D.1
  • 101
    • 0032696092 scopus 로고    scopus 로고
    • Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme
    • Zhang, W., Williams, C.J., Hagan, K. & Peltz, S.W. Mutations in VPS16 and MRT1 stabilize mRNAs by activating an inhibitor of the decapping enzyme. Mol. Cell. Biol. 19, 7568-7576 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7568-7576
    • Zhang, W.1    Williams, C.J.2    Hagan, K.3    Peltz, S.W.4
  • 102
    • 0032832577 scopus 로고    scopus 로고
    • Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover
    • Zuk, D., Belk, J.P. & Jacobson, A. Temperature-sensitive mutations in the Saccharomyces cerevisiae MRT4, GRC5, SLA2 and THS1 genes result in defects in mRNA turnover. Genetics 153, 35-47 (1999).
    • (1999) Genetics , vol.153 , pp. 35-47
    • Zuk, D.1    Belk, J.P.2    Jacobson, A.3
  • 103
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P. et al. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627 (2000).
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1
  • 104
    • 33749199129 scopus 로고    scopus 로고
    • Genome-wide protein interaction screens reveal functional networds involving Sm-like proteins
    • Fromont-Racine, M. et al. Genome-wide protein interaction screens reveal functional networds involving Sm-like proteins. Yeast 17, 95-110 (2000)
    • (2000) Yeast , vol.17 , pp. 95-110
    • Fromont-Racine, M.1
  • 105
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147 (2002).
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.